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Prions responsible for causing bovine spongiform encephalopathy and similar diseases, including Creutzfeldt–Jakob disease, which infects humans, may actually serve a role in helping brains to develop, according to a report in Journal of Neuroscience. Researchers discovered that prion proteins could be helpful or infectious depending on whether the protein was correctly formed. Normal prions were fundamental in protecting nerves, while misfolded prions caused the infectious diseases.

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The small-ruminant prion disease scrapie, a neurodegenerative condition similar to bovine spongiform encephalopathy, might cause disease in humans, according to a new study in Nature Communications. In an animal study, the research team found the infectious agents were transmissible and the infectious prions were undistinguishable from those that cause sporadic Creutzfeldt-Jakob disease.

A new study has found that misfolded prion proteins that aggregate in human and animal diseases, including scrapie, bovine spongiform encephalopathy and Creutzfeldt-Jakob disease, develop resistance to drugs much like other pathogenic agents. The findings indicate that several drugs targeting different aspects of the disease process may be needed if scientists hope to develop a viable treatment for the devastating neurodegenerative diseases.

Researchers looking at a 12-amino-acid section of human prion protein think they may have stumbled upon a structural anomaly -- tails on hexameric oligomers -- that could play a role in how misfolded prions influence nearby proteins, causing disease within and between species. The infectious forms of prions are believed to wreak havoc in neurological tissue, leading to bovine spongiform encephalopathy and other devastating diseases.

Researchers have found that two drugs already approved for use in humans -- tacrolimus and astemizole -- reduce the amount of prion protein present on cell surfaces by about 70%. Misfolded forms of the proteins are believed to cause such diseases as Creutzfeldt-Jakob disease. Astemizole is the most promising because it is effective at relatively low doses, while tacrolimus can cause neurotoxicity.

Justin Hines, a chemistry professor at Lafayette College, is examining the role chaperone proteins play in prion diseases. Chaperone proteins, when functioning normally, prevent improper protein folding that leads to prion formation, according to Hines. The study will examine protein misfolding and chaperone proteins in yeast, but the results may shed light on prion diseases in people and animals, including bovine spongiform encephalopathy, variant Creutzfeldt-Jakob disease in people and chronic wasting disease in deer.